ABSTRACT
Surprisingly,all known FPs show are markable structural similarity.Achromophoremoiety,origin ofÀuorescence,is auto catalytically generated within the conservedβ-barreltertiary structure following asubsequential cyclization andoxidation of an internal tripeptidesequence;for many variants,further reactions can take place,increasing the variety of chromophore structures.A©ner tuning originates from then on covalent interactions of these chromophore structures with the surrounding molecular matrix.§estructure-dependent variety of the optical response is surely one of the factors that have contributed to the success of FPs.Indeed,careful engineering of the protein sequence has enabled tailoring FPs to speci©c imaging techniques in cells.§etunability of FPs upon sequence engineering and careful sequence of the parent protein structure and chromophore represents a challenging,andvery stimulating, ©eld for all bioscientists interested in structure-property relationships in biomolecules.
